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The effects of hydrostatic pressure on the structure and stability of porcine odorant-binding protein (pOBP) in the presence and absence of the odorant molecule 2-isobutyl-3-methoxypyrazine (IBMP) were studied by steady-state and time-resolved fluorescence spectroscopy as well as by molecular dynamics
The mouse major urinary protein (MUP) has proved to be an intriguing test bed for detailed studies on protein-ligand recognition. NMR, calorimetric, and modeling investigations have revealed that the thermodynamics of ligand binding involve a complex interplay between competing enthalpic
Journal of agricultural and food chemistry, 56(22), 10838-10846 (2008-10-24)
The effects of light exposure on 3-isobutyl-2-methoxypyrazine (IBMP) accumulation and degradation in Vitis vinifera L. cv. Cabernet Franc berries were assessed by comparison of shaded and exposed clusters within the same vine throughout a growing season. Twenty-seven vines were shoot-thinned
Journal of the American Chemical Society, 127(33), 11827-11834 (2005-08-18)
In the present study we examine the enthalpy of binding of 2-methoxy-3-isobutylpyrazine (IBMP) to the mouse major urinary protein (MUP), using a combination of isothermal titration calorimetry (ITC), NMR, X-ray crystallography, all-atom molecular dynamics simulations, and site-directed mutagenesis. Global thermodynamics
Journal of biomolecular NMR, 38(1), 3-9 (2007-03-08)
The internal dynamics of recombinant Major Urinary Protein (rMUP) have been investigated by monitoring transverse nitrogen-15 relaxation using multiple-echo Carr-Purcell-Meiboom-Gill (CPMG) experiments. While the ligand-free protein (APO-rMUP) features extensive evidence of motions on the milliseconds time scale, the complex with
Separation of 2-Isopropyl-3-methoxypyrazine 20 ppt; 2-Isobutyl-3-methoxypyrazine; 2-Methylisoborneol; (±)-Geosmin 10 ppt
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